BDBC1_BACAN
ID BDBC1_BACAN Reviewed; 139 AA.
AC Q81UU9; Q6I332; Q6KWV1;
DT 25-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 25-MAY-2022, entry version 125.
DE RecName: Full=Probable disulfide formation protein C 1;
DE AltName: Full=Disulfide oxidoreductase C 1;
DE AltName: Full=Thiol-disulfide oxidoreductase C 1;
GN Name=bdbC1; OrderedLocusNames=BA_0758, GBAA_0758, BAS0722;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Required for disulfide bond formation in some proteins.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Multi-pass membrane
CC protein {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the DsbB family. BdbC subfamily. {ECO:0000305}.
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DR EMBL; AE016879; AAP24768.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT29865.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT53049.1; -; Genomic_DNA.
DR RefSeq; NP_843282.1; NC_003997.3.
DR RefSeq; WP_000532259.1; NZ_WXXJ01000017.1.
DR RefSeq; YP_026998.1; NC_005945.1.
DR AlphaFoldDB; Q81UU9; -.
DR STRING; 261594.GBAA_0758; -.
DR DNASU; 1088398; -.
DR EnsemblBacteria; AAP24768; AAP24768; BA_0758.
DR EnsemblBacteria; AAT29865; AAT29865; GBAA_0758.
DR GeneID; 45020836; -.
DR KEGG; ban:BA_0758; -.
DR KEGG; bar:GBAA_0758; -.
DR KEGG; bat:BAS0722; -.
DR PATRIC; fig|198094.11.peg.758; -.
DR eggNOG; COG1495; Bacteria.
DR HOGENOM; CLU_128688_0_0_9; -.
DR OMA; INWFGFI; -.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0015035; F:protein-disulfide reductase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006457; P:protein folding; IEA:InterPro.
DR Gene3D; 1.20.1550.10; -; 1.
DR HAMAP; MF_00287; BdbC; 1.
DR InterPro; IPR003752; DiS_bond_form_DsbB/BdbC.
DR InterPro; IPR012187; Disulphide_bond_form_BdbC.
DR InterPro; IPR023380; DsbB-like_sf.
DR PANTHER; PTHR43469; PTHR43469; 1.
DR Pfam; PF02600; DsbB; 1.
DR PIRSF; PIRSF036659; BdbC; 1.
DR SUPFAM; SSF158442; SSF158442; 1.
PE 3: Inferred from homology;
KW Cell membrane; Chaperone; Disulfide bond; Electron transport; Membrane;
KW Oxidoreductase; Redox-active center; Reference proteome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..139
FT /note="Probable disulfide formation protein C 1"
FT /id="PRO_0000059370"
FT TRANSMEM 8..27
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 42..61
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 68..85
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TRANSMEM 113..135
FT /note="Helical"
FT /evidence="ECO:0000255"
FT DISULFID 37..40
FT /note="Redox-active"
FT /evidence="ECO:0000250"
FT DISULFID 99..104
FT /note="Redox-active"
FT /evidence="ECO:0000250"
SQ SEQUENCE 139 AA; 15587 MW; 06E658429921C417 CRC64;
MGREKKQEYA LFTAWGASFI ATLGSLYFSE IMKFEPCVLC WYQRIFMYPF VLWLGIAVVK
KDYRIASYSL PIASIGACIS LYHYVIQKVA AFSAAGAACG RVPCTGEYIN WFGFVTIPFL
ALIGFITIAV CSFIVIKNK
